ArticlePloS one2012
Five different piscidins from Nile tilapia, Oreochromis niloticus: analysis of their expressions and biological functions.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 142 citations in OpenAlex.
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- Effects of dietary antimicrobial peptides on growth performance, antioxidant capacity, immune response and disease resistance of juvenile Nile tilapia (Frontiers in physiology · 2026Article
- Marine bioactive peptides as potential therapeutic agents for wound healing - a review.Annals of medicine · 2025Review
- Marine Antimicrobial Peptides: Emerging Strategies Against Multidrug-Resistant and Biofilm-Forming Bacteria.Antibiotics (Basel, Switzerland) · 2025Review
- Designing of a novel chimeric antimicrobial peptide againstResearch in pharmaceutical sciences · 2025Article
- The Evaluation of Teleost-Derived Antimicrobial Peptides Against Neisseria gonorrhoeae.Cureus · 2024Article
- Bacterial diseases in marine fish species: current trends and future prospects in disease management.World journal of microbiology & biotechnology · 2023Review
- Oreoch-1: A Peptide fromPathogens (Basel, Switzerland) · 2023Article
- An Update on the Therapeutic Potential of Antimicrobial Peptides againstPharmaceuticals (Basel, Switzerland) · 2023Review
- Membrane-Active Peptides and Their Potential Biomedical Application.Pharmaceutics · 2023Review
- Exploring Oceans for Curative Compounds: Potential New Antimicrobial and Anti-Virulence Molecules againstMarine drugs · 2022Review
- Investigations on the Wound Healing Potential of Tilapia Piscidin (TP)2-5 and TP2-6.Marine drugs · 2022Article
- Expression of the Antimicrobial Peptide Piscidin 1 and Neuropeptides in Fish Gill and Skin: A Potential Participation in Neuro-Immune Interaction.Marine drugs · 2022Review
- The lipid components of high-density lipoproteins (HDL) are essential for the binding and transportation of antimicrobial peptides in human serum.Scientific reports · 2022Article
- Development of Bactericidal Peptides against Multidrug-ResistantInternational journal of molecular sciences · 2022Article
- Development of Disease-Resistance-Associated Microsatellite DNA Markers for Selective Breeding of Tilapia (Genes · 2021Article
- Marine Transcriptomics Analysis for the Identification of New Antimicrobial Peptides.Marine drugs · 2021Article
- Copper-binding anticancer peptides from the piscidin family: an expanded mechanism that encompasses physical and chemical bilayer disruption.Scientific reports · 2021Article
- Identification of potential therapeutic antimicrobial peptides against Acinetobacter baumannii in a mouse model of pneumonia.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Piscidins are antimicrobial peptides (AMPs) that play important roles in helping fish resist pathogenic infections. Through comparisons of tilapia EST clones, the coding sequences of five piscidin-like AMPs (named TP1∼5) of Nile tilapia, Oreochromis niloticus, were determined. The complete piscidin coding sequences of TP1, -2, -3, -4, and -5 were respectively composed of 207, 234, 231, 270, and 195 bases, and each contained a translated region of 68, 77, 76, 89, and 64 amino acids. The tissue-specific, Vibrio vulnificus stimulation-specific, and Streptococcus agalactiae stimulation-specific expressions of TP2, -3, and -4 mRNA were determined by a comparative RT-PCR. Results of the tissue distribution analysis revealed high expression levels of TP2 mRNA in the skin, head kidneys, liver, and spleen. To study bacterial stimulation, S. agalactiae (SA47) was injected, and the TP4 transcript was upregulated by >13-fold (compared to the wild-type (WT) control, without injection) and was 60-fold upregulated (compared to the WT control, without injection) 24 h after the S. agalactiae (SA47) injection in the spleen and gills. Synthesized TP3 and TP4 peptides showed antimicrobial activities against several bacteria in this study, while the synthesized TP1, -2, and -5 peptides did not. The synthesized TP2, -3, and -4 peptides showed hemolytic activities and synthesized TP3 and TP4 peptides inhibited tilapia ovary cell proliferation with a dose-dependent effect. In summary, the amphiphilic α-helical cationic peptides of TP3 and TP4 may represent novel and potential antimicrobial agents for further peptide drug development.
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